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dc.creatorMargetić, Aleksandra
dc.creatorVujčić, Zoran
dc.date.accessioned2019-09-09T11:50:54Z
dc.date.available2017-11-18
dc.date.issued2017
dc.identifier.issn1082-6068
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/3066
dc.description.abstractYeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60 degrees C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60 degrees C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70 degrees C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.en
dc.publisherTaylor & Francis Inc, Philadelphia
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172048/RS//
dc.rightsembargoedAccess
dc.sourcePreparative Biochemistry & Biotechnology
dc.subjectCell wall invertaseen
dc.subjectenzyme stabilityen
dc.subjectmethanolen
dc.subjectSaccharomyces cerevisiaeen
dc.subjectureaen
dc.titleComparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiaeen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractМаргетић, Aлександра; Вујчић, Зоран;
dc.citation.volume47
dc.citation.issue3
dc.citation.spage305
dc.citation.epage311
dc.citation.other47(3): 305-311
dc.citation.rankM23
dc.description.otherThis is a peer-reviewed version of the article: [https://doi.org/10.1080/10826068.2016.1244683]
dc.description.other[http://cer.ihtm.bg.ac.rs/handle/123456789/2185]
dc.identifier.pmid27737610
dc.identifier.doi10.1080/10826068.2016.1244683
dc.identifier.fulltexthttp://cer.ihtm.bg.ac.rs/bitstream/id/13754/10.108010826068.2016.1244683.pdf
dc.identifier.scopus2-s2.0-85014952387
dc.identifier.wos000396051000012
dc.type.versionacceptedVersion


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